PKG1_ADE02
ID PKG1_ADE02 Reviewed; 449 AA.
AC P03272;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Packaging protein 1 {ECO:0000255|HAMAP-Rule:MF_04057};
DE AltName: Full=Packaging protein IVa2 {ECO:0000255|HAMAP-Rule:MF_04057};
GN Name=IVa2 {ECO:0000255|HAMAP-Rule:MF_04057};
OS Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=10515;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7142161; DOI=10.1016/s0021-9258(18)33473-2;
RA Gingeras T.R., Sciaky D., Gelinas R.E., Bing-Dong J., Yen C.E., Kelly M.M.,
RA Bullock P.A., Parsons B.L., O'Neill K.E., Roberts R.J.;
RT "Nucleotide sequences from the adenovirus-2 genome.";
RL J. Biol. Chem. 257:13475-13491(1982).
RN [2]
RP SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=8627656; DOI=10.1128/jvi.70.3.1396-1405.1996;
RA Lutz P., Kedinger C.;
RT "Properties of the adenovirus IVa2 gene product, an effector of late-phase-
RT dependent activation of the major late promoter.";
RL J. Virol. 70:1396-1405(1996).
RN [3]
RP FUNCTION.
RX PubMed=15327897; DOI=10.1016/j.virol.2004.06.011;
RA Pardo-Mateos A., Young C.S.;
RT "Adenovirus IVa2 protein plays an important role in transcription from the
RT major late promoter in vivo.";
RL Virology 327:50-59(2004).
RN [4]
RP INTERACTION WITH PACKAGING PROTEIN 3.
RX PubMed=15681437; DOI=10.1128/jvi.79.4.2366-2374.2005;
RA Perez-Romero P., Tyler R.E., Abend J.R., Dus M., Imperiale M.J.;
RT "Analysis of the interaction of the adenovirus L1 52/55-kilodalton and IVa2
RT proteins with the packaging sequence in vivo and in vitro.";
RL J. Virol. 79:2366-2374(2005).
RN [5]
RP INTERACTION WITH THE PACKAGING SEQUENCE.
RX PubMed=17229683; DOI=10.1128/jvi.02097-06;
RA Tyler R.E., Ewing S.G., Imperiale M.J.;
RT "Formation of a multiple protein complex on the adenovirus packaging
RT sequence by the IVa2 protein.";
RL J. Virol. 81:3447-3454(2007).
RN [6]
RP INTERACTION WITH PACKAGING PROTEIN 2.
RX PubMed=17804492; DOI=10.1128/jvi.01470-07;
RA Ewing S.G., Byrd S.A., Christensen J.B., Tyler R.E., Imperiale M.J.;
RT "Ternary complex formation on the adenovirus packaging sequence by the IVa2
RT and L4 22-kilodalton proteins.";
RL J. Virol. 81:12450-12457(2007).
RN [7]
RP ATP-BINDING.
RX PubMed=18667504; DOI=10.1128/jvi.00882-08;
RA Ostapchuk P., Hearing P.;
RT "Adenovirus IVa2 protein binds ATP.";
RL J. Virol. 82:10290-10294(2008).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18614642; DOI=10.1128/jvi.01024-08;
RA Christensen J.B., Byrd S.A., Walker A.K., Strahler J.R., Andrews P.C.,
RA Imperiale M.J.;
RT "Presence of the adenovirus IVa2 protein at a single vertex of the mature
RT virion.";
RL J. Virol. 82:9086-9093(2008).
RN [9]
RP FUNCTION.
RX PubMed=20621673; DOI=10.1016/j.virusres.2010.05.013;
RA Backstrom E., Kaufmann K.B., Lan X., Akusjarvi G.;
RT "Adenovirus L4-22K stimulates major late transcription by a mechanism
RT requiring the intragenic late-specific transcription factor-binding site.";
RL Virus Res. 151:220-228(2010).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=21450831; DOI=10.1128/jvi.02538-10;
RA Ostapchuk P., Almond M., Hearing P.;
RT "Characterization of empty adenovirus particles assembled in the absence of
RT a functional adenovirus IVa2 protein.";
RL J. Virol. 85:5524-5531(2011).
RN [11]
RP DNA-BINDING.
RX PubMed=22884292; DOI=10.1016/j.virol.2012.07.013;
RA Christensen J.B., Ewing S.G., Imperiale M.J.;
RT "Identification and characterization of a DNA binding domain on the
RT adenovirus IVa2 protein.";
RL Virology 433:124-130(2012).
RN [12]
RP REVIEW.
RX PubMed=22754652; DOI=10.3390/v4050847;
RA San Martin C.;
RT "Latest insights on adenovirus structure and assembly.";
RL Viruses 4:847-877(2012).
CC -!- FUNCTION: Component of the packaging machinery which encapsidates the
CC viral DNA into preformed capsids and transcriptional activator of the
CC viral major late promoter (MLP). Binds, along with packaging proteins 2
CC and 3, to the specific packaging sequence on the left end of viral
CC genomic DNA and displays ATPase activity thereby providing the power
CC stroke of the packaging machinery. The activity of packaging protein
CC IVa2 is stimulated by protein 33K which acts as a terminase. May be the
CC protein that pumps DNA into the capsid powered by ATP hydrolysis.
CC Specifically binds to the 5'-CG-3' nucleotides of the repeats making up
CC the packaging sequence. Component of the DEF-A and DEF-B transcription
CC factors that bind downstream elements of the major late promoter (MLP),
CC and stimulate transcription from the MLP after initiation of viral DNA
CC replication. DEF-A is a heterodimer packaging proteins 1 and 2 and DEF-
CC B is a homodimer of packaging protein 1. {ECO:0000255|HAMAP-
CC Rule:MF_04057, ECO:0000305|PubMed:15327897,
CC ECO:0000305|PubMed:18614642, ECO:0000305|PubMed:20621673,
CC ECO:0000305|PubMed:8627656}.
CC -!- SUBUNIT: Homodimer (PubMed:8627656). Part of a genome packaging complex
CC composed of packaging proteins 1, 2 and 3; this complex specifically
CC binds to the packaging sequence on the left end of viral genomic DNA
CC and performs packaging of the viral genome (PubMed:15681437,
CC PubMed:17804492). Interacts with protein 33K (By similarity).
CC {ECO:0000250|UniProtKB:P03271, ECO:0000255|HAMAP-Rule:MF_04057,
CC ECO:0000269|PubMed:15681437, ECO:0000269|PubMed:17229683,
CC ECO:0000269|PubMed:17804492, ECO:0000269|PubMed:8627656}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04057,
CC ECO:0000269|PubMed:18614642}. Host nucleus, host nucleoplasm
CC {ECO:0000255|HAMAP-Rule:MF_04057, ECO:0000269|PubMed:8627656}. Host
CC nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04057,
CC ECO:0000269|PubMed:8627656}. Note=Located at a unique vertex of the
CC capsid. Present in about 6-8 copies per virion. {ECO:0000255|HAMAP-
CC Rule:MF_04057, ECO:0000269|PubMed:18614642}.
CC -!- INDUCTION: Expressed in the intermediate phase of the viral replicative
CC cycle. {ECO:0000255|HAMAP-Rule:MF_04057}.
CC -!- DISRUPTION PHENOTYPE: Empty capsids are produced in the absence of
CC packaging protein 1. {ECO:0000269|PubMed:21450831}.
CC -!- SIMILARITY: Belongs to the adenoviridae packaging protein 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_04057}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J01917; AAA92205.1; -; Genomic_DNA.
DR PIR; B03842; Q4ADA2.
DR RefSeq; AP_000165.1; AC_000007.1.
DR RefSeq; NP_040515.1; NC_001405.1.
DR GeneID; 5739974; -.
DR KEGG; vg:5739974; -.
DR Proteomes; UP000008167; Genome.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0044095; C:host cell nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0039708; P:nuclear capsid assembly; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0019073; P:viral DNA genome packaging; IMP:UniProtKB.
DR GO; GO:0098035; P:viral DNA genome packaging via site-specific sequence recognition; IDA:UniProtKB.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04057; ADV_PKG1; 1.
DR InterPro; IPR003389; Adeno_IVa2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02456; Adeno_IVa2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Activator; ATP-binding; DNA-binding; Host nucleus; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Viral genome packaging;
KW Viral release from host cell; Virion.
FT CHAIN 1..449
FT /note="Packaging protein 1"
FT /id="PRO_0000221883"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..449
FT /note="DNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04057,
FT ECO:0000269|PubMed:22884292"
FT COMPBIAS 28..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04057,
FT ECO:0000269|PubMed:18667504"
SQ SEQUENCE 449 AA; 50881 MW; C01EF76D2E5012DC CRC64;
METRGRRPAA LQHQQDQPQA HPGQRAARSA PLHRDPDYAD EDPAPVERHD PGPSGRAPTT
AVQRKPPQPA KRGDMLDRDA VEHVTELWDR LELLGQTLKS MPTADGLKPL KNFASLQELL
SLGGERLLAH LVRENMQVRD MLNEVAPLLR DDGSCSSLNY QLQPVIGVIY GPTGCGKSQL
LRNLLSSQLI SPTPETVFFI APQVDMIPPS ELKAWEMQIC EGNYAPGPDG TIIPQSGTLR
PRFVKMAYDD LILEHNYDVS DPRNIFAQAA ARGPIAIIMD ECMENLGGHK GVSKFFHAFP
SKLHDKFPKC TGYTVLVVLH NMNPRRDMAG NIANLKIQSK MHLISPRMHP SQLNRFVNTY
TKGLPLAISL LLKDIFRHHA QRSCYDWIIY NTTPQHEALQ WCYLHPRDGL MPMYLNIQSH
LYHVLEKIHR TLNDRDRWSR AYRARKTPK
